The objective of the overall research in this laboratory is centered on achieving as complete a description as possible for the structures of peptides, proteins, nucleic acids and their complexes in solution, principally by NMR spectroscopy. At present particular emphasis is being placed on developing approaches which allow the investigation of larger and complex systems as well as increase the precision with which these solution structures can be obtained, studies aimed at correlating structure and function, and experiments aimed at investigating protein folding. Structures for several proteins have been determined and analyzed. These include oxidized and reduced human thioredoxin, the oligomerization domain of p53, the cytokine hMIP-1-beta, and the Ascaris trypsin inhibitor. These studies have exploited many novel 3D and 4D heteronuclear NMR experiments to dramatically increase spectral resolution and thereby resolve assignment ambiguities in larger proteins. The site of interaction of interleukin-8 with the N-terminal cytoplasmic portion of its cell surface receptor has been identified, and the dynamics of the IgG binding domain of Streptococcal G have been investigated. Finally, the folding pathway and kinetics of the highly stable small IgG binding domain of Streptococcal protein G has been studied.